DLDH1_GEOSE
ID DLDH1_GEOSE Reviewed; 470 AA.
AC P11959;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of pyruvate complex;
GN Name=pdhD;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=2200674; DOI=10.1111/j.1432-1033.1990.tb19128.x;
RA Hawkins C.F., Borges A., Perham R.N.;
RT "Cloning and sequence analysis of the genes encoding the alpha and beta
RT subunits of the E1 component of the pyruvate dehydrogenase multienzyme
RT complex of Bacillus stearothermophilus.";
RL Eur. J. Biochem. 191:337-346(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=2253629; DOI=10.1111/j.1432-1033.1990.tb19432.x;
RA Borges A., Hawkins C.F., Packman L.C., Perham R.N.;
RT "Cloning and sequence analysis of the genes encoding the dihydrolipoamide
RT acetyltransferase and dihydrolipoamide dehydrogenase components of the
RT pyruvate dehydrogenase multienzyme complex of Bacillus
RT stearothermophilus.";
RL Eur. J. Biochem. 194:95-102(1990).
RN [3]
RP PROTEIN SEQUENCE OF 41-56.
RX PubMed=6896188; DOI=10.1016/0014-5793(82)80839-9;
RA Packman L.C., Perham R.N.;
RT "An amino acid sequence in the active site of lipoamide dehydrogenase from
RT Bacillus stearothermophilus.";
RL FEBS Lett. 139:155-158(1982).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD, AND SUBUNIT.
RX PubMed=8805537; DOI=10.1016/s0969-2126(96)00032-9;
RA Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.;
RT "Protein-protein interactions in the pyruvate dehydrogenase multienzyme
RT complex: dihydrolipoamide dehydrogenase complexed with the binding domain
RT of dihydrolipoamide acetyltransferase.";
RL Structure 4:277-286(1996).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC dehydrogenase complexes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homodimer. Identified in a complex with PdhC.
CC {ECO:0000269|PubMed:8805537}.
CC -!- INTERACTION:
CC P11959; P11961: pdhC; NbExp=3; IntAct=EBI-9021392, EBI-1040691;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X53560; CAA37631.1; -; Genomic_DNA.
DR PIR; S13839; S13839.
DR PDB; 1EBD; X-ray; 2.60 A; A/B=7-461.
DR PDBsum; 1EBD; -.
DR AlphaFoldDB; P11959; -.
DR SMR; P11959; -.
DR DIP; DIP-6155N; -.
DR IntAct; P11959; 1.
DR BRENDA; 1.8.1.4; 623.
DR EvolutionaryTrace; P11959; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT CHAIN 1..470
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068015"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 39..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8805537"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8805537"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8805537"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8805537"
FT DISULFID 47..52
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 85..108
FT /evidence="ECO:0007829|PDB:1EBD"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 233..246
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1EBD"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 322..336
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:1EBD"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:1EBD"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1EBD"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 419..432
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:1EBD"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:1EBD"
SQ SEQUENCE 470 AA; 49356 MW; C9C05F21A3EE4CB7 CRC64;
MVVGDFAIET ETLVVGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALIS
ASHRYEQAKH SEEMGIKAEN VTIDFAKVQE WKASVVKKLT GGVEGLLKGN KVEIVKGEAY
FVDANTVRVV NGDSAQTYTF KNAIIATGSR PIELPNFKFS NRILDSTGAL NLGEVPKSLV
VIGGGYIGIE LGTAYANFGT KVTILEGAGE ILSGFEKQMA AIIKKRLKKK GVEVVTNALA
KGAEEREDGV TVTYEANGET KTIDADYVLV TVGRRPNTDE LGLEQIGIKM TNRGLIEVDQ
QCRTSVPNIF AIGDIVPGPA LAHKASYEGK VAAEAIAGHP SAVDYVAIPA VVFSDPECAS
VGYFEQQAKD EGIDVIAAKF PFAANGRALA LNDTDGFLKL VVRKEDGVII GAQIIGPNAS
DMIAELGLAI EAGMTAEDIA LTIHAHPTLG EIAMEAAEVA LGTPIHIITK
